Abstract

Background The CD4-binding site (CD4BS) on HIV-1 gp120 is functionally conserved and structurally invariant, and the broadly neutralizing antibody b12 exploits this site of vulnerability to achieve neutralization. However, most antibodies that target this general epitope cannot effectively neutralize HIV-1. Why is HIV-1 resistant to neutralization by these antibodies? Comparison at the atomic level of gp120 binding to effective and non-effective antibodies may reveal the answer.

Highlights

  • Open AccessCrystal structure of gp120 in complex with the CD4-binding-site antibody b13 suggests precise targeting is needed for neutralization

  • The CD4-binding site (CD4BS) on HIV-1 gp120 is functionally conserved and structurally invariant, and the broadly neutralizing antibody b12 exploits this site of vulnerability to achieve neutralization

  • Our results suggest that targeting of the CD4-binding site by an antibody which slightly misses the precise site of CD4 attachment results in a cascade of conformational changes in gp120

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Summary

Open Access

Crystal structure of gp120 in complex with the CD4-binding-site antibody b13 suggests precise targeting is needed for neutralization. Address: 1Vaccine Research Center, NIAID/NIH, Bethesda, MD, USA and 2The Scripps Research Institute, La Jolla, CA, USA * Corresponding author from AIDS Vaccine 2009 Paris, France. Published: 22 October 2009 Retrovirology 2009, 6(Suppl 3):P66 doi:10.1186/1742-4690-6-S3-P66. AIDS Vaccine 2009 Anna Laura Ross Meeting abstracts – A single PDF containing all abstracts in this Supplement is available here. http://www.biomedcentral.com/content/pdf/1471-2105-10-S12-info.pdf

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